4zgy

STRUCTURE of HUMAN ORNITHINE DECARBOXYLASE IN COMPLEX WITH A C-TERMINAL FRAGMENT OF ANTIZYME

Method: X-RAY DIFFRACTION Dmax: 82.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ornithine decarboxylase

Homo sapiens

UniProt P11926

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–421 Fragment:UNP RESIDUES 2-421 Ornithine decarboxylase antizyme 1 × 1 (P54368) PLP PYRIDOXAL-5'-PHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;100MM MAGNESIUM ACETATE, 50MM MES PH 5.6, 20% 2-METHYL-2, 4-PENTANEDIOL(MPD), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K Resolution 2.63 Å R-free 0.256

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCOR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–422; UniProt 2–421

Ornithine decarboxylase antizyme 1

Homo sapiens

UniProt P54368

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 95–219 Fragment:UNP RESIDUES 95-219 Ornithine decarboxylase × 1 (P11926) PLP PYRIDOXAL-5'-PHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;100MM MAGNESIUM ACETATE, 50MM MES PH 5.6, 20% 2-METHYL-2, 4-PENTANEDIOL(MPD), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K Resolution 2.63 Å R-free 0.256

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OAZ1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 11–135; UniProt 95–219

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4zgy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4zgy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4zgy
Deposition date deposition_date2015-04-24
Structure title titleSTRUCTURE of HUMAN ORNITHINE DECARBOXYLASE IN COMPLEX WITH A C-TERMINAL FRAGMENT OF ANTIZYME
Keywords keywordsTIM-BARREL DOMAIN, BETA-SHEET DOMAIN, DECARBOXYLATION, ANTIZYME, PLASMA, LYASE-LYASE INHIBITOR COMPLEX; LYASE/LYASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.18
Radius of gyration Rg (electron density) rg_electron24.18
Forward intensity I(0) i050572000.00
Molecular weight molecular_weight56410.0 kDa
Excluded volume excluded_volume71094 ų
Envelope volume envelope_volume87479 ų
Hydration-shell volume shell_volume29788 ų
Envelope diameter envelope_diameter85.5
Shell Rg shell_rg31.78
Envelope Rg envelope_rg24.69
Shape Rg shape_rg24.17
Total Rg total_rg25.09
Total atoms total_atoms3970
Residues n_residues508
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax82.4
Rg (real space) rg_real25.13
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real5.0570e+07
I(0) uncertainty (real space) i0_real_error7.4670e+05
Rg (reciprocal space) rg_reciprocal25.14
I(0) (reciprocal space) i0_reciprocal50570000.0000
Solution quality estimate total_estimate0.8860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17680000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4zgyb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamilyd.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family familyd.108.1.7 — Ornithine decarboxylase antizyme-like

CATH v4.4 (3 domains)

Domain ID domain_id4zgyA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology37 — Lyase, Ornithine Decarboxylase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Lyase, Ornithine Decarboxylase; Chain A, domain 1
Domain ID domain_id4zgyA02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily10 — Alanine racemase
Domain ID domain_id4zgyB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)